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anti trail r2 antibody  (Novus Biologicals)
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Novus Biologicals anti trail r2 antibody
Figure 4 4HPR does not change the levels of proteins known to modulate <t>TRAIL-mediated</t> apoptosis. (a) Cell lines were incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h. Cell lysates were prepared and immunoblotted for TRAIL-R1 and <t>TRAIL-R2</t> as indicated to the right of the panel. To control for specificity, lysates from 293T cells transfected with vector (V), TRAIL-R1 (R1), or TRAIL-R2 (R2) were included on the immunoblots. Tubulin is shown as a loading control for each paired sample. The heavy arrows indicate the positions of the predominant species of TRAIL-R1 or TRAIL-R2. The light arrows indicate the position of alternative protein species (see text for discussion). (b) The A224 and A547 cell lines were incubated as above. The total surface TRAIL binding was determined by measuring GST-TRAIL or GST binding with an fluorescein isothiocyanate (FITC)-conjugated anti-GST antibody by flow cytometry. The surface expression of TRAIL-R1 and TRAIL-R2 was determined by measuring the binding of anti-TRAIL-R1, anti-TRAIL-R2, or isotype-matched IgG antibody (as a control) with an FITC-conjugated antibody by flow cytometry. The upper, middle, and bottom panels represent the total surface expression, the TRAIL-R1 and TRAIL-R2 surface expression, respectively. The curves represent the control and the surface expression upon medium and 4HPR incubation. (c) Cell lysates from cells incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h were immunobloted for TRAIL-R3, TRAIL-R4, FLIP, IAP-1, IAP-2, XIAP, and Survivin as indicated to the right of the panel. Tubulin is shown as a loading control for each paired sample. TRAIL-R3 was not detected in these cell lines and so is not shown. Molecular weights in kDa are shown to the left of the panels. Arrows indicate positions of each protein
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Figure 4 4HPR does not change the levels of proteins known to modulate TRAIL-mediated apoptosis. (a) Cell lines were incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h. Cell lysates were prepared and immunoblotted for TRAIL-R1 and TRAIL-R2 as indicated to the right of the panel. To control for specificity, lysates from 293T cells transfected with vector (V), TRAIL-R1 (R1), or TRAIL-R2 (R2) were included on the immunoblots. Tubulin is shown as a loading control for each paired sample. The heavy arrows indicate the positions of the predominant species of TRAIL-R1 or TRAIL-R2. The light arrows indicate the position of alternative protein species (see text for discussion). (b) The A224 and A547 cell lines were incubated as above. The total surface TRAIL binding was determined by measuring GST-TRAIL or GST binding with an fluorescein isothiocyanate (FITC)-conjugated anti-GST antibody by flow cytometry. The surface expression of TRAIL-R1 and TRAIL-R2 was determined by measuring the binding of anti-TRAIL-R1, anti-TRAIL-R2, or isotype-matched IgG antibody (as a control) with an FITC-conjugated antibody by flow cytometry. The upper, middle, and bottom panels represent the total surface expression, the TRAIL-R1 and TRAIL-R2 surface expression, respectively. The curves represent the control and the surface expression upon medium and 4HPR incubation. (c) Cell lysates from cells incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h were immunobloted for TRAIL-R3, TRAIL-R4, FLIP, IAP-1, IAP-2, XIAP, and Survivin as indicated to the right of the panel. Tubulin is shown as a loading control for each paired sample. TRAIL-R3 was not detected in these cell lines and so is not shown. Molecular weights in kDa are shown to the left of the panels. Arrows indicate positions of each protein

Journal: Cell death and differentiation

Article Title: N-(4-hydroxyphenyl) retinamide (4HPR) enhances TRAIL-mediated apoptosis through enhancement of a mitochondrial-dependent amplification loop in ovarian cancer cell lines.

doi: 10.1038/sj.cdd.4401387

Figure Lengend Snippet: Figure 4 4HPR does not change the levels of proteins known to modulate TRAIL-mediated apoptosis. (a) Cell lines were incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h. Cell lysates were prepared and immunoblotted for TRAIL-R1 and TRAIL-R2 as indicated to the right of the panel. To control for specificity, lysates from 293T cells transfected with vector (V), TRAIL-R1 (R1), or TRAIL-R2 (R2) were included on the immunoblots. Tubulin is shown as a loading control for each paired sample. The heavy arrows indicate the positions of the predominant species of TRAIL-R1 or TRAIL-R2. The light arrows indicate the position of alternative protein species (see text for discussion). (b) The A224 and A547 cell lines were incubated as above. The total surface TRAIL binding was determined by measuring GST-TRAIL or GST binding with an fluorescein isothiocyanate (FITC)-conjugated anti-GST antibody by flow cytometry. The surface expression of TRAIL-R1 and TRAIL-R2 was determined by measuring the binding of anti-TRAIL-R1, anti-TRAIL-R2, or isotype-matched IgG antibody (as a control) with an FITC-conjugated antibody by flow cytometry. The upper, middle, and bottom panels represent the total surface expression, the TRAIL-R1 and TRAIL-R2 surface expression, respectively. The curves represent the control and the surface expression upon medium and 4HPR incubation. (c) Cell lysates from cells incubated in medium supplemented with ( þ ) or without () 4HPR at 1 mM for 96 h were immunobloted for TRAIL-R3, TRAIL-R4, FLIP, IAP-1, IAP-2, XIAP, and Survivin as indicated to the right of the panel. Tubulin is shown as a loading control for each paired sample. TRAIL-R3 was not detected in these cell lines and so is not shown. Molecular weights in kDa are shown to the left of the panels. Arrows indicate positions of each protein

Article Snippet: Rabbit polyclonal anti-caspase 3 specific for the procaspase 3 or for the 18 kDa cleavage product (1 mg/ml; BD PharMingen, San Diego, CA, USA), anti-caspase 9 (1 mg/ml; Cell Signalling, Beverly, MA, USA), anti-PARP antibody (1 mg/ml; H-250, Santa Cruz Biotechnology), anti-TRAIL-R1 antibody (1mg/ml; BD PharMingen, San Diego, CA, , USA), anti-TRAIL-R2 antibody (1 mg/ml; Imgenex, San Diego, CA, USA), anti-TRAIL-R3 antibody (1 mg/ml; Affinity bioreagents, Golden, CO, USA), anti-TRAIL-R4 antibody (1 mg/ml; Oncogene Research Products, Cambridge, MA, USA), anti-IAP-1 antibody (1 mg/ ml; R&D Systems Inc., Minneapolis, MN, USA), anti-IAP-2 antibody (1.5 mg/ml; R&D Systems Inc.), anti-FLIP antibody (2 mg/ml; Calbiochem), anti-survivin antibody (1mg/ml; R&D Systems Inc.), anti-erk-2 antibody (1mg/ml; C-14, Santa Cruz Biotechnology), anti Smac/DIABLO (1mg/ml; Imgenex), mouse monoclonal anti-caspase 7 (1 mg/ml; BD PharMingen), anti-caspase 8 (1mg/ml; clone 5F7, Upstate Biotechnology, Lake Placid, NY, USA), anti-XIAP antibody (2 mg/ml; BD PharMingen), anti-cytochrome c antibody (1mg/ml; BD PharMingen), anti-FLAG (10 mg/ml; clone M5, Sigma Chemical Co.), anti-a-tubulin antibody (0.5 mg/ml; Sigma Chemical Co.), goat polyclonal anti-caspase 10 (1mg/ml; C-16, Santa Cruz Biotechnology, Santa Cruz, CA, USA), and anti-BID antibody (1mg/ml; C-20, Santa Cruz Biotechnology) were used for immunoblotting.

Techniques: Incubation, Control, Transfection, Plasmid Preparation, Western Blot, Binding Assay, Cytometry, Expressing

Figure 5 Combination of 4HPR and TRAIL activates caspase-8 and -9. (a) The AD10 cell line was incubated with or without 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the indicated times. Cell lysates were prepared and immunoblotted with caspase-8, caspase-9, cleaved caspase-3, and erk-2 as indicated to the right of the panels. The procaspases and their cleaved products are indicated by the arrows to the right of the panels. The panels showing procaspase-8 and its cleavage product are from a short and long exposure of the same filter, respectively. Erk-2 is shown as a loading control. (b) The AD10 cell line was incubated with 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the final 16 h in culture. Cell lysates were prepared and immunoblotted with caspase-3, caspase-7, caspase-3, BID, and PARP as indicated to the right of the panels. The procaspases and the full-length form of PARP (p116) are indicated by arrows to the right of the panels. p85 and p25 are the cleaved PARP products. Erk-2 is shown as a loading control. Molecular weights in kDa is show to the right of the panels. (c) Caspase assays were performed on the cell lysates treated with TRAIL for 6 h in panel (a) with the indicated substrates. Activity for each substrate was normalized to the activity in the untreated cells and the data represent the mean7S.D. for triplicate measurements from a representative experiment. (d) The AD10 cell line was incubated with 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the indicated times. Cell lysates were prepared and immunoblotted with caspase-8 and erk-2 as indicated to the right of the panels. Procaspase-8 (p55) and its cleaved products are indicated by the arrows to the right of the panels. The panel showing the 18 kDa cleavage product of caspase-8 is from a longer exposure of the same filter shown in the upper panel. Erk-2 is shown as a loading control. (e) Lysates for AD10 cells treated with either TRAIL or the combination of TRAIL and 4HPR for 3 h were precipitated using GST-TRAIL or GST as indicated, and the lysates were evaluated for the presence of TRAIL-R1, TRAIL-R2, and procaspase-8 by immunoblotting as indicated

Journal: Cell death and differentiation

Article Title: N-(4-hydroxyphenyl) retinamide (4HPR) enhances TRAIL-mediated apoptosis through enhancement of a mitochondrial-dependent amplification loop in ovarian cancer cell lines.

doi: 10.1038/sj.cdd.4401387

Figure Lengend Snippet: Figure 5 Combination of 4HPR and TRAIL activates caspase-8 and -9. (a) The AD10 cell line was incubated with or without 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the indicated times. Cell lysates were prepared and immunoblotted with caspase-8, caspase-9, cleaved caspase-3, and erk-2 as indicated to the right of the panels. The procaspases and their cleaved products are indicated by the arrows to the right of the panels. The panels showing procaspase-8 and its cleavage product are from a short and long exposure of the same filter, respectively. Erk-2 is shown as a loading control. (b) The AD10 cell line was incubated with 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the final 16 h in culture. Cell lysates were prepared and immunoblotted with caspase-3, caspase-7, caspase-3, BID, and PARP as indicated to the right of the panels. The procaspases and the full-length form of PARP (p116) are indicated by arrows to the right of the panels. p85 and p25 are the cleaved PARP products. Erk-2 is shown as a loading control. Molecular weights in kDa is show to the right of the panels. (c) Caspase assays were performed on the cell lysates treated with TRAIL for 6 h in panel (a) with the indicated substrates. Activity for each substrate was normalized to the activity in the untreated cells and the data represent the mean7S.D. for triplicate measurements from a representative experiment. (d) The AD10 cell line was incubated with 4HRP (1 mM) for a total of 48 h and TRAIL (250 ng/ml) was added for the indicated times. Cell lysates were prepared and immunoblotted with caspase-8 and erk-2 as indicated to the right of the panels. Procaspase-8 (p55) and its cleaved products are indicated by the arrows to the right of the panels. The panel showing the 18 kDa cleavage product of caspase-8 is from a longer exposure of the same filter shown in the upper panel. Erk-2 is shown as a loading control. (e) Lysates for AD10 cells treated with either TRAIL or the combination of TRAIL and 4HPR for 3 h were precipitated using GST-TRAIL or GST as indicated, and the lysates were evaluated for the presence of TRAIL-R1, TRAIL-R2, and procaspase-8 by immunoblotting as indicated

Article Snippet: Rabbit polyclonal anti-caspase 3 specific for the procaspase 3 or for the 18 kDa cleavage product (1 mg/ml; BD PharMingen, San Diego, CA, USA), anti-caspase 9 (1 mg/ml; Cell Signalling, Beverly, MA, USA), anti-PARP antibody (1 mg/ml; H-250, Santa Cruz Biotechnology), anti-TRAIL-R1 antibody (1mg/ml; BD PharMingen, San Diego, CA, , USA), anti-TRAIL-R2 antibody (1 mg/ml; Imgenex, San Diego, CA, USA), anti-TRAIL-R3 antibody (1 mg/ml; Affinity bioreagents, Golden, CO, USA), anti-TRAIL-R4 antibody (1 mg/ml; Oncogene Research Products, Cambridge, MA, USA), anti-IAP-1 antibody (1 mg/ ml; R&D Systems Inc., Minneapolis, MN, USA), anti-IAP-2 antibody (1.5 mg/ml; R&D Systems Inc.), anti-FLIP antibody (2 mg/ml; Calbiochem), anti-survivin antibody (1mg/ml; R&D Systems Inc.), anti-erk-2 antibody (1mg/ml; C-14, Santa Cruz Biotechnology), anti Smac/DIABLO (1mg/ml; Imgenex), mouse monoclonal anti-caspase 7 (1 mg/ml; BD PharMingen), anti-caspase 8 (1mg/ml; clone 5F7, Upstate Biotechnology, Lake Placid, NY, USA), anti-XIAP antibody (2 mg/ml; BD PharMingen), anti-cytochrome c antibody (1mg/ml; BD PharMingen), anti-FLAG (10 mg/ml; clone M5, Sigma Chemical Co.), anti-a-tubulin antibody (0.5 mg/ml; Sigma Chemical Co.), goat polyclonal anti-caspase 10 (1mg/ml; C-16, Santa Cruz Biotechnology, Santa Cruz, CA, USA), and anti-BID antibody (1mg/ml; C-20, Santa Cruz Biotechnology) were used for immunoblotting.

Techniques: Incubation, Control, Activity Assay, Western Blot